Proteomics Peptides & KitsPeptide sets and pools, as well as assay standardization kits are available with stable isotope labeled or unlabeled proteotypic peptides for mass-spectrometry based proteomics such as MRM assays.

Chelate Peptides (DOTA)DOTA is linked to molecules that have affinity for various structures (e.g. somatostatin receptors in neuroendocrine tumors). The resulting compounds can be bound to radionuclided and are used with a number of radioisotopes in cancer therapy and diagnosis

Immunology Standards & ControlsStandards and controls for reproducible T-cell assays such as ELISPOT and multimer assays. We offer a large variety of positive and negative control peptide pools for antigen specific T cell stimulation as well as kit to produce TCR-engineered reference samples for performance control.

Antigen PeptidesAntigen peptides represent specific epitopes for stimulation of T cells in T cell assays such as ELISPOT. We offer the corresponding MHC multimer for each antigen peptide. Antigens from different pathogens are available as well as tumor associated antigens.

Cosmetic PeptidesCosmetic Peptides such as Lysine and Cysteine Peptide are used for DPRA (Direct Peptide Reactivity Assay) for Skin Sensitization Testing. The DPRA measures the reaction of a chemical with synthetic peptides containing Cysteine (Ac‑RFAACAA‑COOH) or Lysine (Ac‑RFAAKAA‑COOH) to assess its sensitization potency. For research use only!

Putting Polyphosphates to the Test: Evidence Against Platelet-Induced Activation of Factor XII

Faxälv et al., Blood (2013) - PMID: 23896408

The recent claim that stimulated platelets activate the intrinsic pathway of coagulation by the release of polyphosphates has been considered a breakthrough in hemostasis research. In little more than 3 years, the original publication by Müller et al has been cited >100 times. However, none of the citing articles has sought to independently validate this potentially paradigm-shifting concept. To this end, we performed extensive experimentation in vitro and in vivo in an attempt to verify the claim that factor XII (FXII) is primarily activated by stimulated platelets. In contrast to the original assertion, platelet-derived polyphosphates were found to be weak activators of FXII, with a FXIIa-generating activity of <10% compared with equivalent concentrations of kaolin. Using different coagulation assays, it was shown that platelet contribution to whole blood coagulation was unrelated to the generation of activated FXII in vitro. Additionally, key results used to verify the hypothesis in the original study in vivo were found to be irreproducible. We conclude that platelet-derived polyphosphates are not physiologically relevant activators of FXII.